001458 - Multisensitization to Chicken, Turkey, Rooster and Whey Proteins: Molecular Allergen Characterization by IgE–Western Blot

Allergy to poultry meat is uncommon, and its coexistence with sensitization to additional animal-derived proteins is even more unusual. In such complex profiles, the identification of specific allergenic molecules is essential to distinguish true multisensitization from cross-reactivity and to inform targeted dietary recommendations. IgE–Western blot is particularly valuable in this context, as it allows direct visualization of IgE-binding proteins under native and denatured conditions.

A 45-year-old man reported oral allergy symptoms after ingestion of chicken, turkey, rooster (Zeus faber), goat cheese and whey-protein supplements, while maintaining tolerance to cow’s milk, cheeses and other fish species. Skin prick tests with commercial extracts were negative; however, prick-by-prick tests were positive for raw and cooked chicken and turkey, rooster, whey protein powder and goat cheese. Total IgE was 154 kU/L, and specific IgE was positive for cow, goat and sheep milk, as well as α-lactalbumin, β-lactoglobulin and casein.Protein extracts from chicken, turkey, rooster (raw and cooked) and whey were prepared and analyzed by SDS-PAGE followed by IgE–Western blot under reducing and non-reducing conditions.

SDS-PAGE demonstrated marked differences between raw and cooked samples. IgE–Western blot analysis revealed IgE binding to a ~40 kDa protein in raw chicken consistent with aldolase; ~37 kDa and ~70 kDa proteins in raw turkey corresponding to serum albumin and a thermolabile protein; multiple whey proteins including ~12 kDa (α-lactalbumin), 14–16 kDa (β-lactoglobulin) and ~27 kDa (casein); and a ~19 kDa heat-stable protein in cooked rooster compatible with parvalbumin. The combined findings indicate sensitizations to structurally unrelated proteins across species rather than a shared cross-reactive allergen.

This case illustrates a rare pattern of independent sensitizations to multiple animal-derived proteins, involving aldolase, serum albumin and parvalbumin. The distinct thermal stability of these proteins—thermolabile albumins versus heat-stable parvalbumins—correlates with the patient’s clinical responses to raw and cooked foods. IgE–Western blot proved essential for accurately defining the molecular basis of the patient’s reactions and underscores the diagnostic importance of detailed immunochemical assessment in atypical multisource food allergy.